Nucleic Acids Research, 2002, Vol. 30, No. 4 975-982
© 2002 Oxford University Press
c-Maf, the 
D-crystallin Maf-responsive element and growth factor regulation
Department of Biochemistry, University of Nijmegen, Nijmegen, The Netherlands
The transcription factor c-Maf has been suggested to regulate the activity of 
-crystallin promoters in lens fibre cells. We here show that the transactivation potential of c-Maf and MafB for the rat D-crystallin Maf-responsive element (D MARE) is dependent upon the cellular context and, using chimeric and single domain mutants, that c-Maf is most likely to be the cognate factor for the D MARE in the lens. Transactivation of the D MARE by c-Maf in lens cells was not enhanced by c-Fos or c-Jun and was not blocked by dominant negative c-Fos or c-Jun constructs. c-Maf can activate the D MARE as a homodimer since activation of the D-crystallin promoter in P19 embryonic carcinoma cells required only c-Maf, but none of a number of c-Fos and c-Jun family members tested. Transactivation by c-Maf was inhibited by activation of protein kinase A (PKA) (by signal transduction agonist forskolin) or of protein kinase C (PKC) (by signal transduction agonist tetradecanoyl phorbol acetate). Site-directed mutagenesis showed that this effect is not mediated by phosphorylation of the consensus PKA/PKC site in the extended DNA-binding domain, but likely involves activation of MAP kinase kinase, as inhibition by PD98059 increased transactivation by c-Maf.
* To whom correspondence should be addressed at: Biochemistry 161, NCMLS, PO Box 9101, 6500 HB Nijmegen, The Netherlands. Tel: +31 24 3616850; Fax: +31 24 3540525; Email: nhl{at}sci.kun.nl
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